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Journal Article

Ionics and conformational transitions of Na,K-ATPase

MPS-Authors
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Grell,  Ernst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Warmuth,  Ralf
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Lewitzki,  Erwin
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Ruf,  Horst
Molecular Biophysics Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Grell, E., Warmuth, R., Lewitzki, E., & Ruf, H. (1992). Ionics and conformational transitions of Na,K-ATPase. Acta Physiologica Scandinavica, 607, 213-221.


Cite as: https://hdl.handle.net/21.11116/0000-0008-4ADC-E
Abstract
Equilibrium binding studies have been carried out by spectrofluorometric precision titrations on FITC-Na,K-ATPase and employing the styryl dye RH-421 to obtain equilibrium constants and stoichiometric coefficients together with information related to competition between different binding equilibria. A new interpretation concerning the assignment of spectral properties and cation complex formation equilibria, as well as the involvement of conformational transitions, is suggested, based on a differentiation between selective and unselective alkali ion binding. The kinetics of K+ binding to the FITC-enzyme have been studied by employing a new microvolume technique consisting of flash photolysis of caged-K+.